ArticleCell cycle (Georgetown, Tex.)2008
Modulation of 14-3-3 interaction with phosphorylated histone H3 by combinatorial modification patterns.
Article in Cell cycle (Georgetown, Tex.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 50 citations in OpenAlex.
- Potential 14-3-3 binding sites in sirtuins reveal extended phosphosite-recognition modes.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Benzaldehyde suppresses epithelial-mesenchymal plasticity and overcomes treatment resistance in cancer by targeting the interaction of 14-3-3ζ with H3S28ph.British journal of cancer · 2025Article
- Deubiquitinating enzyme mutagenesis screens identify a USP43-dependent HIF-1 transcriptional response.The EMBO journal · 2024Article
- Comparative analysis of methods to reduce activation signature gene expression in PBMCs.Scientific reports · 2023Article
- Coordinated histone modifications and chromatin reorganization in a single cell revealed by FRET biosensors.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Epigenomic Modifications Mediating Antibody Maturation.Frontiers in immunology · 2018Review
- Mitogen-induced distinct epialleles are phosphorylated at either H3S10 or H3S28, depending on H3K27 acetylation.Molecular biology of the cell · 2017Article
- Identification of protein complexes that bind to histone H3 combinatorial modifications using super-SILAC and weighted correlation network analysis.Nucleic acids research · 2015Article
- H3S28 phosphorylation is a hallmark of the transcriptional response to cellular stress.Genome research · 2014Article
- Sensing core histone phosphorylation - a matter of perfect timing.Biochimica et biophysica acta · 2014Review
- The Heterochromatin-1 Phosphorylation Contributes to TPA-Induced AP-1 Expression.Biomolecules & therapeutics · 2014Article
- The Ah receptor recruits IKKα to its target binding motifs to phosphorylate serine-10 in histone H3 required for transcriptional activation.Toxicological sciences : an official journal of the Society of Toxicology · 2014Article
- Combinatorial H3K9acS10ph histone modification in IgH locus S regions targets 14-3-3 adaptors and AID to specify antibody class-switch DNA recombination.Cell reports · 2013Article
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- Molecular Modeling of Differentially Phosphorylated Serine 10 and Acetylated lysine 9/14 of Histone H3 Regulates their Interactions with 14-3-3ζ, MSK1, and MKP1.Bioinformatics and biology insights · 2013Article
- Histone H3 phosphorylation - a versatile chromatin modification for different occasions.Biochimie · 2012Review
- New partners in regulation of gene expression: the enhancer of Trithorax and Polycomb Corto interacts with methylated ribosomal protein l12 via its chromodomain.PLoS genetics · 2012Article
- Global analysis of the relationship between JIL-1 kinase and transcription.PLoS genetics · 2011Article
- A phosphorylation switch regulates the transcriptional activation of cell cycle regulator p21 by histone deacetylase inhibitors.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Post-translational modifications of histones are determining factors in the global and local regulation of genome activity. Phosphorylation of histone H3 is globally associated with mitotic chromatin compaction but occurs in a much more restricted manner during interphase transcriptional regulation of a limited subset of genes. In the course of gene regulation, serine 10 phosphorylation at histone H3 is targeted to a very small fraction of nucleosomes that is highly susceptible to additional acetylation events. Recently, we and others have identified 14-3-3 as a binding protein that recognizes both phosphorylated serine 10 and phosphorylated serine 28 on histone H3. In vitro, the affinity of 14-3-3 for phosphoserine 10 is weak but becomes significantly increased by additional acetylation of either lysine 9 or lysine 14 on the same histone tail. In contrast, the histone H3S28 site matches elements of 14-3-3 high affinity consensus motifs. This region mediates an initial stronger interaction that is less susceptible to modulation by "auxiliary" modifications. Here we discuss the binding of 14-3-3 proteins to histone H3 in detail and putative biological implications of these interactions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.